2QPT

Crystal structure of an EHD ATPase involved in membrane remodelling

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005901	cellular_component	caveola
A	0006897	biological_process	endocytosis
A	0010008	cellular_component	endosome membrane
A	0015630	cellular_component	microtubule cytoskeleton
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019904	molecular_function	protein domain specific binding
A	0030866	biological_process	cortical actin cytoskeleton organization
A	0032456	biological_process	endocytic recycling
A	0042802	molecular_function	identical protein binding
A	0045171	cellular_component	intercellular bridge
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0055038	cellular_component	recycling endosome membrane
A	0072659	biological_process	protein localization to plasma membrane
A	0097320	biological_process	plasma membrane tubulation
A	1901741	biological_process	positive regulation of myoblast fusion
A	2001137	biological_process	positive regulation of endocytic recycling

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 700

Chain	Residue
A	THR72
A	THR94
A	ANP600

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 701

Chain	Residue
A	ASP494
A	ASP496
A	ASP498
A	MET500
A	GLU505

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site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP A 600

Chain	Residue
A	SER68
A	THR69
A	GLY70
A	LYS71
A	THR72
A	SER73
A	VAL88
A	GLY89
A	THR93
A	THR94
A	GLY156
A	ASN219
A	LYS220
A	SER256
A	PHE257
A	TRP258
A	MG700
A	TYR67

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Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DVDRDGMLDdeEF

Chain	Residue	Details
A	ASP494-PHE506

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342, ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID

Chain	Residue	Details
A	GLY65
A	TRP258

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:24508342, ECO:0007744|PDB:4CID

Chain	Residue	Details
A	LYS220

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342, ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID

Chain	Residue	Details
A	ASP494
A	ASP496
A	ASP498
A	MET500
A	GLU505

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q4V8H8

Chain	Residue	Details
A	SER3
A	SER493

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER44
A	SER468

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER438

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9NZN4

Chain	Residue	Details
A	SER470
A	SER484

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